ID S4XW68_SORCE Unreviewed; 1151 AA.
AC S4XW68;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Nitric oxide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCE1572_10085 {ECO:0000313|EMBL:AGP34833.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP34833.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP34833.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP34833.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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DR EMBL; CP003969; AGP34833.1; -; Genomic_DNA.
DR AlphaFoldDB; S4XW68; -.
DR STRING; 1254432.SCE1572_10085; -.
DR KEGG; scu:SCE1572_10085; -.
DR PATRIC; fig|1254432.3.peg.2263; -.
DR eggNOG; COG1018; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR eggNOG; COG4362; Bacteria.
DR eggNOG; COG5126; Bacteria.
DR HOGENOM; CLU_274956_0_0_7; -.
DR Proteomes; UP000014803; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:InterPro.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR CDD; cd00322; FNR_like; 1.
DR CDD; cd00575; NOS_oxygenase; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 177..212
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 214..246
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 518..620
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1151 AA; 125414 MW; 3DE1CC15C231C63E CRC64;
MSFLKIVCSE PKNDLASFLQ SLPIEPAEPV VALVLSTADL AYPHVAARTF VASAKEVGAS
HLLWVAPYVP PSSRLGQQIR DAEAFVRASG HRVTAVWHGP LLSALNLWRE DIRLRRTLPL
PLGSAALPWV APADVARMAI RALEQPGVEA PVVRGPAACT GAEVAAALSR AVRAALASER
FAWRRFEEID RDNNRALSED ELLPYLTGLG IPADEARALL VAADTTGDGT LDFEEFTAGL
RGPLDNLVQQ LLREDTFEIR YVDTPADRAV AALVQAGLRR AAAEALVEGW ASVAAEGIPE
GPDEAWLELP PASVDAWAER HALDYVNVHL LPGQGLLSQR EATVEDGAAM GALAGKPAAV
SSIVDGGGRI LTLFRALDGS GVSARWRDAP AESLRWVTCG DRDKRRALLV SGGQLAGVHV
EGEWQGLPSA MRQLMARAPL PGWQLATFRE LGELKLEQSA ALCEPHEVVC NCAGVKRGQI
TGLIEGGCAT VAELSERTRA GQICGGCVPA IEEMFGGSSL VQAEVKGARE VAPGIFQIAL
SPVGGAPAAS VPGQHVLVQG YLDRRWVARA YTLSAPARAG GDYEITVKRE ELGVFSRWLC
ERAAASLLRA SAPRGSFVLP APPVERVVFL AGGIGVTPAM AMLRALDGRA DRAEARAFLL
DWSASRAADF LYFEEELRAI AGRTPGVALR LRATQAEGRL SGEDVVELYP YRPGSRALVC
GPDGFMRDAH EHLRAAGWPA DAIQRELFTS NVDVAGTIRQ APLRRAGAVR AAGGVCPVEH
GSFHLTPTAS AAALTEAEAF LRQCYAELGV PSAVDERWQE VRASLEKHGT YTHLPDELAY
GARLAWRNSS RCIGRFFWST LHVRDLRHLT TEEEIFQALV EHLDLATNGG DIRATMSVFR
PGEPRIRIWN GQLARYAGYR LPDGGILGDP ANVELTDQAL ALGWPGGERT RFDLLPLIIQ
IGDARPRWFE LPRERVLEVP IEHPRHAWFA ELGLKWHALP AVCNLALDLG GIHYTAAPFN
GFYMGTEIGA RNLSDATRYN QLPLIADRLG LDRSRSDTLW QDAALVELNI AVLHSFRQAK
VRMLDHHTLS EYFKKFEQQE RQCERPVYAD WSWIVPPMSA STMAVFHTNM ENKILKPNYL
YQDDPWKERK G
//
